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Volumn 163, Issue 2, 2009, Pages 85-94

Identification of a thrombospondin-like immunodominant and phosphorylcholine-containing glycoprotein (GP300) in Dictyocaulus viviparus and related nematodes

Author keywords

Dictyocaulus viviparus; Lungworm; N glycan; Phosphorylcholine; Thrombospondin; Wheat germ agglutinin

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN 300; PHOSPHORYLCHOLINE; PROTEINASE; THROMBOSPONDIN; UNCLASSIFIED DRUG;

EID: 57849159697     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2008.09.012     Document Type: Article
Times cited : (13)

References (45)
  • 1
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glyco-epitopes, core α(1,3)-fucose and core xylose
    • Bardor M., Faveeuw C., Fitchette A.C., et al. Immunoreactivity in mammals of two typical plant glyco-epitopes, core α(1,3)-fucose and core xylose. Glycobiology 13 (2003) 427-434
    • (2003) Glycobiology , vol.13 , pp. 427-434
    • Bardor, M.1    Faveeuw, C.2    Fitchette, A.C.3
  • 2
    • 0033233118 scopus 로고    scopus 로고
    • Core alpha 1 → 3 fucose is a common modification of N-glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonconchus contortus infected sheep
    • van Die I., Gomord V., Kooyman F.N., et al. Core alpha 1 → 3 fucose is a common modification of N-glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonconchus contortus infected sheep. FEBS Lett 463 (1999) 189-193
    • (1999) FEBS Lett , vol.463 , pp. 189-193
    • van Die, I.1    Gomord, V.2    Kooyman, F.N.3
  • 3
    • 10644221237 scopus 로고    scopus 로고
    • Structure and synthesis of nematodes phosphorylcholine-containing glycoconjugates
    • Houston K.M., and Harnett W. Structure and synthesis of nematodes phosphorylcholine-containing glycoconjugates. Parasitology 129 (2004) 655-661
    • (2004) Parasitology , vol.129 , pp. 655-661
    • Houston, K.M.1    Harnett, W.2
  • 4
    • 0033783188 scopus 로고    scopus 로고
    • Phosphorylcholine substituents in nematodes: structures, occurrence and biological implications
    • Lochnit G., Dennis R.D., and Geyer R. Phosphorylcholine substituents in nematodes: structures, occurrence and biological implications. Biol Chem 381 (2000) 839-847
    • (2000) Biol Chem , vol.381 , pp. 839-847
    • Lochnit, G.1    Dennis, R.D.2    Geyer, R.3
  • 5
    • 0032834853 scopus 로고    scopus 로고
    • Immunogenic, glycoconjugates implicated in parasitic nematode diseases
    • Dell A.S., Haslam S.M., Morris H.R., and Khoo K.H. Immunogenic, glycoconjugates implicated in parasitic nematode diseases. Biochim Biophys Acta 1455 (1999) 353-362
    • (1999) Biochim Biophys Acta , vol.1455 , pp. 353-362
    • Dell, A.S.1    Haslam, S.M.2    Morris, H.R.3    Khoo, K.H.4
  • 6
    • 1642554719 scopus 로고    scopus 로고
    • Immune biasing by helminths glycans
    • Thomas P.G., and Harn Jr. D.A. Immune biasing by helminths glycans. Cell Microbiol 6 (2004) 13-22
    • (2004) Cell Microbiol , vol.6 , pp. 13-22
    • Thomas, P.G.1    Harn Jr., D.A.2
  • 7
    • 33745191896 scopus 로고    scopus 로고
    • Filarial nematode secreted product ES-62 is an anti-inflammatory agent: therapeutic potential of small molecule derivates and ES-62 peptide mimetics
    • Harnett W., and Harnett M.M. Filarial nematode secreted product ES-62 is an anti-inflammatory agent: therapeutic potential of small molecule derivates and ES-62 peptide mimetics. Clin Exp Pharmacol Physiol 33 (2006) 511-518
    • (2006) Clin Exp Pharmacol Physiol , vol.33 , pp. 511-518
    • Harnett, W.1    Harnett, M.M.2
  • 8
    • 35948948204 scopus 로고    scopus 로고
    • Inhibition of FcepsilonRI-mediated mast cell responses by ES-62, a product of parasitic filarial nematodes
    • Melendez A.J., Harnett M.M., Pushparaj P.N., et al. Inhibition of FcepsilonRI-mediated mast cell responses by ES-62, a product of parasitic filarial nematodes. Nat Med 13 (2007) 1375-1381
    • (2007) Nat Med , vol.13 , pp. 1375-1381
    • Melendez, A.J.1    Harnett, M.M.2    Pushparaj, P.N.3
  • 9
    • 0033857664 scopus 로고    scopus 로고
    • Presence of phosphorylcholine on a filarial nematode protein influences immunoglobulin G subclass response to the molecule by an interleukin-10-dependent mechanism
    • Houston K.M., Wilson E.H., Eyres L., et al. Presence of phosphorylcholine on a filarial nematode protein influences immunoglobulin G subclass response to the molecule by an interleukin-10-dependent mechanism. Infect Immun 68 (2000) 5466-5468
    • (2000) Infect Immun , vol.68 , pp. 5466-5468
    • Houston, K.M.1    Wilson, E.H.2    Eyres, L.3
  • 10
    • 41849107589 scopus 로고    scopus 로고
    • The phosphorylcholine moiety of the filarial nematode immunomodulator ES-62 is responsible for its anti-inflammatory action in arthritis
    • Harnett M.M., Kean D.E., Boitelle A., et al. The phosphorylcholine moiety of the filarial nematode immunomodulator ES-62 is responsible for its anti-inflammatory action in arthritis. Ann Rheum Dis 67 (2008) 518-523
    • (2008) Ann Rheum Dis , vol.67 , pp. 518-523
    • Harnett, M.M.1    Kean, D.E.2    Boitelle, A.3
  • 11
    • 33846921268 scopus 로고    scopus 로고
    • Phosphorylcholine mimics the effects of ES-62 on macrophages and dendritic cells
    • Goodridge H.S., McGuiness S., Houston K.M., et al. Phosphorylcholine mimics the effects of ES-62 on macrophages and dendritic cells. Par Immunol 29 (2007) 127-137
    • (2007) Par Immunol , vol.29 , pp. 127-137
    • Goodridge, H.S.1    McGuiness, S.2    Houston, K.M.3
  • 12
    • 0032746382 scopus 로고    scopus 로고
    • Molecular cloning and demonstration of an aminopeptidase activity in a filarial nematode glycoprotein
    • Harnett W., Houston K.M., Tate R., et al. Molecular cloning and demonstration of an aminopeptidase activity in a filarial nematode glycoprotein. Mol Biochem Parasitol 104 (1999) 11-23
    • (1999) Mol Biochem Parasitol , vol.104 , pp. 11-23
    • Harnett, W.1    Houston, K.M.2    Tate, R.3
  • 13
    • 0024746127 scopus 로고
    • Origin, kinetics of circulation and fate in vivo of the major excretory-secretory product of Acanthocheilonema viteae
    • Harnett W., Worms M.J., Kapil A., Grainger M., and Parkhouse R.M. Origin, kinetics of circulation and fate in vivo of the major excretory-secretory product of Acanthocheilonema viteae. Parasitology 99 (1989) 229-239
    • (1989) Parasitology , vol.99 , pp. 229-239
    • Harnett, W.1    Worms, M.J.2    Kapil, A.3    Grainger, M.4    Parkhouse, R.M.5
  • 14
    • 0000146825 scopus 로고
    • Immunological studies on Dictyocaulus viviparus infection. The immunity resulting from experimental infection
    • Jarrett W.F., Jennings F.W., McIntyre W.I., et al. Immunological studies on Dictyocaulus viviparus infection. The immunity resulting from experimental infection. Immunology 2 (1959) 252-261
    • (1959) Immunology , vol.2 , pp. 252-261
    • Jarrett, W.F.1    Jennings, F.W.2    McIntyre, W.I.3
  • 15
    • 0001691692 scopus 로고
    • Immunological studies on Dictyocaulus viviparus infection. Immunity produced by the administration of irradiated larvae
    • Jarrett W.F., Jennings F.W., McIntyre W.I., Mulligan W., and Urquhart G.M. Immunological studies on Dictyocaulus viviparus infection. Immunity produced by the administration of irradiated larvae. Immunology 3 (1960) 145-151
    • (1960) Immunology , vol.3 , pp. 145-151
    • Jarrett, W.F.1    Jennings, F.W.2    McIntyre, W.I.3    Mulligan, W.4    Urquhart, G.M.5
  • 16
    • 0000868461 scopus 로고
    • Immunological studies on Dictyocaulus viviparus infection. Passive immunisation
    • Jarrett W.F., Jennings H.F., McIntyre W.I., Mulligan W., and Urquhart G.M. Immunological studies on Dictyocaulus viviparus infection. Passive immunisation. Vet Rec 67 (1955) 291-296
    • (1955) Vet Rec , vol.67 , pp. 291-296
    • Jarrett, W.F.1    Jennings, H.F.2    McIntyre, W.I.3    Mulligan, W.4    Urquhart, G.M.5
  • 17
    • 33846026776 scopus 로고    scopus 로고
    • Differential N-glycan- and protein-directed immune responses in Dictyocaulus viviparus-infected and vaccinated calves
    • Kooyman F.N., Ploeger H.W., Høglund J., and van Putten J.P. Differential N-glycan- and protein-directed immune responses in Dictyocaulus viviparus-infected and vaccinated calves. Parasitology 134 (2007) 269-279
    • (2007) Parasitology , vol.134 , pp. 269-279
    • Kooyman, F.N.1    Ploeger, H.W.2    Høglund, J.3    van Putten, J.P.4
  • 18
    • 0036159823 scopus 로고    scopus 로고
    • Serum immunoglobulin E response in calves infected with the lungworm Dictyocaulus viviparus and its correlation with protection
    • Kooyman F.N., Yatsuda A.P., Ploeger H.W., and Eysker M. Serum immunoglobulin E response in calves infected with the lungworm Dictyocaulus viviparus and its correlation with protection. Par Immunol 24 (2002) 47-56
    • (2002) Par Immunol , vol.24 , pp. 47-56
    • Kooyman, F.N.1    Yatsuda, A.P.2    Ploeger, H.W.3    Eysker, M.4
  • 19
    • 34548487816 scopus 로고    scopus 로고
    • Antibodies elicited by the bovine lungworm, Dictyocaulus viviparus, cross-react with platelet-activating factor
    • Kooyman F.N., de Vries E., Ploeger H.W., and van Putten J.P. Antibodies elicited by the bovine lungworm, Dictyocaulus viviparus, cross-react with platelet-activating factor. Infect Immun 75 (2007) 4456-4462
    • (2007) Infect Immun , vol.75 , pp. 4456-4462
    • Kooyman, F.N.1    de Vries, E.2    Ploeger, H.W.3    van Putten, J.P.4
  • 20
    • 0025521623 scopus 로고
    • Recovery of different stages of Dictyocaulus viviparus from cattle lungs by a combination of a perfusion and Baermann technique
    • Eysker M., Boersema J.H., and Hendrikx W.M. Recovery of different stages of Dictyocaulus viviparus from cattle lungs by a combination of a perfusion and Baermann technique. ResVet Sci 49 (1990) 373-374
    • (1990) ResVet Sci , vol.49 , pp. 373-374
    • Eysker, M.1    Boersema, J.H.2    Hendrikx, W.M.3
  • 21
    • 0035187252 scopus 로고    scopus 로고
    • Characterization of host responser types after a single Cooperia oncophora infection: kinetics of the systemic immune response
    • Kanobana K., Vervelde L., van der Veer M., Eysker M., and Ploeger H.W. Characterization of host responser types after a single Cooperia oncophora infection: kinetics of the systemic immune response. Par Immunol 23 (2001) 641-653
    • (2001) Par Immunol , vol.23 , pp. 641-653
    • Kanobana, K.1    Vervelde, L.2    van der Veer, M.3    Eysker, M.4    Ploeger, H.W.5
  • 22
    • 0034799036 scopus 로고    scopus 로고
    • Cloning and characterization of thrombospondin, a novel multidomain glycoprotein found in association with a host protective gut extract from Haemonchus contortus
    • Skuce P.J., Newlands G.F., Stewart E.M., et al. Cloning and characterization of thrombospondin, a novel multidomain glycoprotein found in association with a host protective gut extract from Haemonchus contortus. Mol Biochem Parasitol 117 (2001) 241-244
    • (2001) Mol Biochem Parasitol , vol.117 , pp. 241-244
    • Skuce, P.J.1    Newlands, G.F.2    Stewart, E.M.3
  • 23
    • 0024542252 scopus 로고
    • Western immunoblotting: temperature-dependent reduction in background staining
    • Thean E.T., and Toh B.H. Western immunoblotting: temperature-dependent reduction in background staining. Anal Biochem 177 (1989) 256-258
    • (1989) Anal Biochem , vol.177 , pp. 256-258
    • Thean, E.T.1    Toh, B.H.2
  • 24
    • 20844458058 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the Schistosoma mansoni tegumental sub-proteome
    • van Balkom A.B., van Gestel W.R.A., Brouwers J.F., et al. Mass spectrometric analysis of the Schistosoma mansoni tegumental sub-proteome. J Proteome Res 4 (2005) 958-966
    • (2005) J Proteome Res , vol.4 , pp. 958-966
    • van Balkom, A.B.1    van Gestel, W.R.A.2    Brouwers, J.F.3
  • 25
    • 33745857712 scopus 로고    scopus 로고
    • In-gel isoelectric focusing of peptides as a tool for improved protein identification
    • Krijgsveld J., Gauci S., Dormeyer W., and Heck A.J. In-gel isoelectric focusing of peptides as a tool for improved protein identification. J Proteome Res 5 (2006) 1721-1730
    • (2006) J Proteome Res , vol.5 , pp. 1721-1730
    • Krijgsveld, J.1    Gauci, S.2    Dormeyer, W.3    Heck, A.J.4
  • 26
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., and Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 27
    • 0033572755 scopus 로고    scopus 로고
    • Isolation, characterization and immunolocalisation of phosphorylcholine-substituted glycolipids in developmental stages of Caenorhabditis elegans
    • Gerdt S., Dennis R.D., Borgonie G., Schnabel R., and Geyer R. Isolation, characterization and immunolocalisation of phosphorylcholine-substituted glycolipids in developmental stages of Caenorhabditis elegans. Eur J Biochem 266 (1999) 952-963
    • (1999) Eur J Biochem , vol.266 , pp. 952-963
    • Gerdt, S.1    Dennis, R.D.2    Borgonie, G.3    Schnabel, R.4    Geyer, R.5
  • 28
  • 30
    • 0034518571 scopus 로고    scopus 로고
    • Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases
    • Kramerova I., Kawaguchi A.N., Fessler L.I., et al. Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases. Development 127 (2000) 5475-5485
    • (2000) Development , vol.127 , pp. 5475-5485
    • Kramerova, I.1    Kawaguchi, A.N.2    Fessler, L.I.3
  • 31
    • 0033214761 scopus 로고    scopus 로고
    • Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta
    • Nardi J.B., Martos R., Walden K.K., Lampe D.J., and Robertson H.M. Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta. Insect Biochem Mol Biol 29 (1999) 883-897
    • (1999) Insect Biochem Mol Biol , vol.29 , pp. 883-897
    • Nardi, J.B.1    Martos, R.2    Walden, K.K.3    Lampe, D.J.4    Robertson, H.M.5
  • 32
    • 16544369169 scopus 로고    scopus 로고
    • Papilin, a novel component of basement membranes, in relation to ADAMTS metalloproteases and ECM development
    • Fessler J.F., Kramerova I., Kramerov A., Chen Y., and Fessler L.I. Papilin, a novel component of basement membranes, in relation to ADAMTS metalloproteases and ECM development. Int J Biochem Cell Biol 36 (2004) 1079-1084
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1079-1084
    • Fessler, J.F.1    Kramerova, I.2    Kramerov, A.3    Chen, Y.4    Fessler, L.I.5
  • 33
    • 0028828338 scopus 로고
    • Shedding of surface-bound antibody by adult Dictyocaulus viviparus
    • McKeand J.B., and Kennedy M.W. Shedding of surface-bound antibody by adult Dictyocaulus viviparus. Int J Parasitol 25 (1995) 1255-1258
    • (1995) Int J Parasitol , vol.25 , pp. 1255-1258
    • McKeand, J.B.1    Kennedy, M.W.2
  • 34
    • 3242772439 scopus 로고    scopus 로고
    • The thrombospondin type 1 repeat superfamily
    • Tucker R.T. The thrombospondin type 1 repeat superfamily. Int J Biochem Cell Biol 36 (2004) 969-974
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 969-974
    • Tucker, R.T.1
  • 35
    • 0034074901 scopus 로고    scopus 로고
    • The thrombospondin type I repeat (TSR) superfamily: diverse proteins with related roles in neuronal development
    • Adams J.C., and Tucker R.P. The thrombospondin type I repeat (TSR) superfamily: diverse proteins with related roles in neuronal development. Dev Dyn 218 (2000) 280-299
    • (2000) Dev Dyn , vol.218 , pp. 280-299
    • Adams, J.C.1    Tucker, R.P.2
  • 36
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski Jr. M., and Kato I. Protein inhibitors of proteinases. Annu Rev Biochem 49 (1980) 593-626
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski Jr., M.1    Kato, I.2
  • 37
    • 0037398198 scopus 로고    scopus 로고
    • Molecular cloning of a novel multidomain kunitz-type proteinase inhibitor from the hookworm Ancylostoma caninum
    • Hawdon J.M., Datu B., and Crowell M. Molecular cloning of a novel multidomain kunitz-type proteinase inhibitor from the hookworm Ancylostoma caninum. J Parasitol 89 (2003) 402-407
    • (2003) J Parasitol , vol.89 , pp. 402-407
    • Hawdon, J.M.1    Datu, B.2    Crowell, M.3
  • 38
    • 0030989415 scopus 로고    scopus 로고
    • Characterization of the phosphorylcholine-containing N-linked oligosaccharides in the excretory-secretory 62 kDa glycoprotein of Acanthocheilonema viteae
    • Haslam S.M., Khoo K.H., Houston K.M., et al. Characterization of the phosphorylcholine-containing N-linked oligosaccharides in the excretory-secretory 62 kDa glycoprotein of Acanthocheilonema viteae. Mol Biochem Parasitol 85 (1997) 53-66
    • (1997) Mol Biochem Parasitol , vol.85 , pp. 53-66
    • Haslam, S.M.1    Khoo, K.H.2    Houston, K.M.3
  • 39
    • 0034022046 scopus 로고    scopus 로고
    • Biocompatibility of phosphorylcholine coated stents in normal porcine coronary arteries
    • Whelan D.M., van der Giessen W.J., Krabbendam S.C., et al. Biocompatibility of phosphorylcholine coated stents in normal porcine coronary arteries. Heart 83 (2006) 338-345
    • (2006) Heart , vol.83 , pp. 338-345
    • Whelan, D.M.1    van der Giessen, W.J.2    Krabbendam, S.C.3
  • 40
    • 0037382329 scopus 로고    scopus 로고
    • Alternative splicing of papilin and the diversity of Drosophila extracellular matrix during embryonic morphogenesis
    • Kramerova I.A., Kramerov A.A., and Fessler J.F. Alternative splicing of papilin and the diversity of Drosophila extracellular matrix during embryonic morphogenesis. Dev Dyn 226 (2003) 634-642
    • (2003) Dev Dyn , vol.226 , pp. 634-642
    • Kramerova, I.A.1    Kramerov, A.A.2    Fessler, J.F.3
  • 41
    • 36348973439 scopus 로고    scopus 로고
    • Gene inactivation confirms the identity of enzymes involved in nematode phosphorylcholine-N-glycan synthesis
    • Houston K.M., Sutharsan R., Steiger C.N., et al. Gene inactivation confirms the identity of enzymes involved in nematode phosphorylcholine-N-glycan synthesis. Mol Biochem Parasitol 157 (2008) 88-91
    • (2008) Mol Biochem Parasitol , vol.157 , pp. 88-91
    • Houston, K.M.1    Sutharsan, R.2    Steiger, C.N.3
  • 42
    • 0029852531 scopus 로고    scopus 로고
    • Haemonchus contortus glycoproteins contain N-linked oligosaccharides with novel highly fucosylated core structures
    • Haslam A.M., Coles G.C., Munn E.A., et al. Haemonchus contortus glycoproteins contain N-linked oligosaccharides with novel highly fucosylated core structures. J Biol Chem 271 (1996) 30561-30570
    • (1996) J Biol Chem , vol.271 , pp. 30561-30570
    • Haslam, A.M.1    Coles, G.C.2    Munn, E.A.3
  • 43
    • 0030895871 scopus 로고    scopus 로고
    • Variation in the nature of attachment of phosphorylcholine to excretory-secretory products of adult Brugia pahangi
    • Nor Z.M., Houston K.M., Devaney E., and Harnett W. Variation in the nature of attachment of phosphorylcholine to excretory-secretory products of adult Brugia pahangi. Parasitology 114 (1997) 257-262
    • (1997) Parasitology , vol.114 , pp. 257-262
    • Nor, Z.M.1    Houston, K.M.2    Devaney, E.3    Harnett, W.4
  • 44
    • 0032485270 scopus 로고    scopus 로고
    • A molecular evolutionary framework for the phylum Nematoda
    • Blaxter M., De Ley P., Garey L.R., et al. A molecular evolutionary framework for the phylum Nematoda. Nature 392 (1998) 71-75
    • (1998) Nature , vol.392 , pp. 71-75
    • Blaxter, M.1    De Ley, P.2    Garey, L.R.3
  • 45
    • 33745146522 scopus 로고    scopus 로고
    • The evolutionary origins of nematodes within the order Strongylida are related to predilection sites within the hosts
    • Chilton N.B., Huby-Chilton F., Gasser R.B., and Beveridge I. The evolutionary origins of nematodes within the order Strongylida are related to predilection sites within the hosts. Mol Phylogenet Evol 40 (2006) 118-128
    • (2006) Mol Phylogenet Evol , vol.40 , pp. 118-128
    • Chilton, N.B.1    Huby-Chilton, F.2    Gasser, R.B.3    Beveridge, I.4


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